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. 2010 Aug 2;30(19):4687–4697. doi: 10.1128/MCB.01581-09

FIG. 7.

FIG. 7.

(A) Interaction between VRK2A and the KSR1 scaffold. 293T cells were transfected with plasmid pCMV-Flag-KSR1 or pCMV-Flag (control) and pCEFL-GST-VRK2A or pCEFL-GST, the cell extract was immunoprecipitated (IP) with an anti-Flag antibody, and the proteins present in the immunoprecipitate were detected with antibodies for the epitopes. For the pulldown (PD) assay, cells were transfected with pCEFL-GST-VRK2A or pCEFL-GST, and endogenous KSR1 was detected with a specific antibody. (B) Interaction of VRK2A with MEK. HEK293T cells were transfected with plasmid pCEFL-GST VRK2A or pCEFL-GST as a control, in combination with plasmid pCEFL-HA-MEK. The lysates were used for pulldown, and proteins (right) were detected by immunoblotting. (C) Direct interaction between endogenous MEK1 and VRK2 proteins in MCF7 cells. Endogenous MEK1 was immunoprecipitated with 9G3 monoclonal antibody (Ab), and the endogenous VRK2 protein present in the immunoprecipitate was detected by Western blotting.